Coordination features and affinity of the Cu²+ site in the α-synuclein protein of Parkinson's disease
about
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicityα-Synuclein mutations cluster around a putative protein loop.Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.ESEEM analysis of multi-histidine Cu(II)-coordination in model complexes, peptides, and amyloid-βThe Methylococcus capsulatus (Bath) secreted protein, MopE*, binds both reduced and oxidized copperClioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity.The N Terminus of α-Synuclein Forms Cu(II)-Bridged Oligomers.Copper(I/II), α/β-Synuclein and Amyloid-β: Menage à Trois?Genome-Wide Analyses of Metal Responsive Genes in Caenorhabditis elegans.Involvement of heat shock proteins on Mn-induced toxicity in Caenorhabditis elegans.α-Synuclein Amyloid Fibrils with Two Entwined, Asymmetrically Associated Protofibrils.Coordination of copper to the membrane-bound form of α-synuclein.Amyloid-β and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing.A novel α-synuclein missense mutation in Parkinson disease.Unique effect of Cu(II) in the metal-induced amyloid formation of β-2-microglobulinRole of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.α-Synuclein Misfolding Versus Aggregation Relevance to Parkinson's Disease: Critical Assessment and Modeling.Reactivity of copper-α-synuclein peptide complexes relevant to Parkinson's disease.The Rich Electrochemistry and Redox Reactions of the Copper Sites in the Cellular Prion Protein.Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics.Cu(II) promotes amyloid pore formation.Conversion of natively unstructured α-synuclein to its α-helical conformation significantly attenuates production of reactive oxygen speciesComparison of the structural characteristics of Cu(2+)-bound and unbound α-syn12 peptide obtained in simulations using different force fields.Peculiarities of copper binding to alpha-synuclein.Aqueous Synthesis of Protein-Encapsulated ZnSe Quantum Dots and Physical Significance of Semiconductor-Induced CuII Ion Sensing.The role of the Cys-X-X-X-Cys motif on the kinetics of cupric ion loading to the Streptomyces lividans Sco protein.Effect of Zn(2+) ions on the assembly of amylin oligomers: insight into the molecular mechanisms.
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P2860
Coordination features and affinity of the Cu²+ site in the α-synuclein protein of Parkinson's disease
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Coordination features and affi ...... protein of Parkinson's disease
@ast
Coordination features and affi ...... protein of Parkinson's disease
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Coordination features and affi ...... protein of Parkinson's disease
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Coordination features and affi ...... protein of Parkinson's disease
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type
label
Coordination features and affi ...... protein of Parkinson's disease
@ast
Coordination features and affi ...... protein of Parkinson's disease
@en
Coordination features and affi ...... protein of Parkinson's disease
@en-gb
Coordination features and affi ...... protein of Parkinson's disease
@nl
prefLabel
Coordination features and affi ...... protein of Parkinson's disease
@ast
Coordination features and affi ...... protein of Parkinson's disease
@en
Coordination features and affi ...... protein of Parkinson's disease
@en-gb
Coordination features and affi ...... protein of Parkinson's disease
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P2093
P2860
P921
P3181
P356
P1433
P1476
Coordination features and affi ...... protein of Parkinson's disease
@en
P2093
Christopher G Dudzik
Eric D Walter
Glenn L Millhauser
P2860
P304
P3181
P356
10.1021/BI101912Q
P407
P577
2011-03-22T00:00:00Z